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New technique helps researchers determine amino-acid charge

d. "Previous work has told us how the helices are oriented in the closed state."

A major problem in understanding the relationship between structure and function in proteins, and the impact that electrostatics have on them, Grosman said, is not knowing the protonation state of ionizable residues. Protons, he added, are so small that they cannot be detected even with X-ray crystallographic approaches.

For the study, Grosman and colleagues used protein engineering. They mutated each residue of the pore's lining with basic amino-acid residues, which can acquire a positive charge upon binding protons and become neutral upon releasing them.

"One thing is the proton affinity of an amino-acid residue when the amino acid is dissolved in a lot of water in, say, a glass beaker; another thing is the affinity for protons in the complex microenvironment presented by a membrane protein," Grosman said. "For the first time, we were able to measure proton-transfer events at the single-proton, single-amino-acid level, in real time. Chemists will be happy to see this."

In addition to providing an extensive set of proton-affinity values for basic residues, which differed greatly from those found in a "glass beaker," the findings also discounted a long-held theory that the rotation of the pore-lining helices underlie the mechanism of opening and closing of the nicotinic receptor ion channel. The data, Grosman said, indicate that such rotation is minimal, if any.


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Source:University of Illinois at Urbana-Champaign


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